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Induction of T cell adhesion to extracellular matrix or endothelial cell ligands by soluble or matrix‐bound interleukin‐7
Author(s) -
Ariel Amiram,
Hershkoviz Rami,
Cahalon Liora,
Williams Douglas E.,
Akiyama Steven K.,
Yamada Kenneth M.,
Chen Chun,
Alon Ronen,
Lapidot Tsvee,
Lider Ofer
Publication year - 1997
Publication title -
european journal of immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.272
H-Index - 201
eISSN - 1521-4141
pISSN - 0014-2980
DOI - 10.1002/eji.1830271015
Subject(s) - fibronectin , extracellular matrix , integrin , microbiology and biotechnology , cell adhesion molecule , cell adhesion , biology , adhesion , cytokine , cell–cell interaction , cell , biochemistry , chemistry , immunology , organic chemistry
Abstract The putative effects of interleukin (IL)‐7, operating in the context of extracellular matrix (ECM), on the adhesion of human T cells were examined. Recombinant human IL‐7 was found to bind ECM or fibronectin (FN) with IC 50 values of 10–100 nM. Nanogram amounts of both soluble and, especially, FN‐ or ECM‐bound IL‐7, which differentially affected the morphologies of FN‐adherent T cells, induced the adhesion of resting CD4 + and CD8 + T cells in dose‐dependent and β1 integrin‐dependent manners. Under static and flow conditions, soluble IL‐7 also induced the binding of unstimulated T cells to vascular cell adhesion molecule‐1, suggesting that this cytokine can also modulate integrin binding to endothelial cell ligands. The effects of affinity modulation by IL‐7 of FN‐specific β1 integrins depend on the presence of soluble FN, which inhibited T cell adhesion to FN induced by FN‐bound IL‐7 or by an integrin‐specific affinity‐modulating monoclonal antibody, but not by soluble IL‐7 or phorbol 12‐myristate 13‐acetate. These findings provide an example of a major ECM integrin ligand, FN, which is capable of modulating its adhesive interactions with specific immune cells by associating with and presenting a cytokine in a bio‐active state.